VGN50 peptide

VGN50 peptide

• Handling and Storage of Synthetic Peptides
• Material Safety Data Sheets (MSDS)

Batch to batch variation of the purity

rKKRR-Orn-RRR-βAla-LSSILQGLYQLDT

H-(D)-Arg-Lys-Lys-Arg-Arg-Orn-Arg-Arg-Arg-βAla-Leu-Ser-Ser-Ile-Leu-Gln-Gly-Leu-Tyr-Gln-Leu-Asp-Thr-OH

22

95.62%

C₁₂₁H₂₁₈N₄₆O₃₂

2827.70

Synthetic

Powder

VGN50 is a peptide derived from the Kaposi's sarcoma-associated herpes virus transactivator (K-Rta) sequence, based on the binding interface of K-Rta and cellular coactivators. VGN50 interacts with components of coactivators including nuclear receptor coactivator 2 (NCOA2), p300, and SWItch/Sucrose Non-Fermentable (SWI/SNF), the subfamily of ATP-dependent chromatin remodeling complex proteins. VGN50 blocks recruitment of the SWI/SNF complex and results in downregulation of both MYC and MYC-target gene transcription. Expression of MYC is tightly regulated in normal cells but becomes dysregulated in many types of human cancer cells, and application of VGN50 can reduce cell proliferation and selectively kill cancer cell lines in both tissue culture and a xenograft tumour mouse model.

Normally, this peptide will be delivered in lyophilized form and should be stored in a freezer at or below -20 °C. For more details, please refer to the manual: Handling and Storage of Synthetic Peptides

• Shimoda et al (2021) KSHV transactivator-derived small peptide traps coactivators to attenuate MYC and inhibits leukemia and lymphoma cell growth. Commun Biol. 4(1) 1330 PMID: 34857874

Trifluoroacetic acid (TFA) has a significant impact on peptides due to its role in the peptide synthesis process.

TFA is essential for the protonation of peptides that lack basic amino acids such as Arginine (Arg), Histidine (His), and Lysine (Lys), or ones that have blocked N-termini. As a result, peptides often contain TFA salts in the final product.

TFA residues, when present in custom peptides, can cause unpredictable fluctuations in experimental data. At a nanomolar (nM) level, TFA can influence cell experiments, hindering cell growth at low concentrations (as low as 10 nM) and promoting it at higher doses (0.5–7.0 mM). It can also serve as an allosteric regulator on the GlyR of glycine receptors, thereby increasing receptor activity at lower glycine concentrations.

In an in vivo setting, TFA can trifluoroacetylate amino groups in proteins and phospholipids, inducing potentially unwanted antibody responses. Moreover, TFA can impact structure studies as it affects spectrum absorption.